alexa Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide.


Journal of Clinical & Experimental Pathology

Author(s): Holmgren A

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Abstract The recent high-resolution solution structures of human and Escherichia coli thioredoxin in their oxidized and reduced states support a catalytic model of protein disulfide reduction involving binding of a target protein and nucleophilic attack by the active-site Cys32 thiolate to form a transition state mixed disulfide.
This article was published in Structure and referenced in Journal of Clinical & Experimental Pathology

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